Evidence map›Paper›PMID 1664238›Full record

ArticleCell regulation1991

Identification of chicken embryo kinase 5, a developmentally regulated receptor-type tyrosine kinase of the Eph family.

E B Pasquale

Open access · greenAbstract read
In one paragraph

Article in Cell regulation, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.3field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 75 citations in OpenAlex.

  1. The Roles of EphB2 in Cancer.Frontiers in cell and developmental biology · 2022
    Review
  2. Article
  3. Article
  4. Eph receptors and ephrins in the developing chick cerebellum: relationship to sagittal patterning and granule cell migration.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000
    Article
  5. Roles of Eph receptors and ephrins in segmental patterning.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2000
    Review
  6. Article
  7. An Eph receptor regulates integrin activity through R-Ras.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  8. Article
  9. Article
  10. Purification of a ligand for the EPH-like receptor HEK using a biosensor-based affinity detection approach.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  11. Embryonic stem cells express multiple Eph-subfamily receptor tyrosine kinases.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Molecular cloning of HEK, the gene encoding a receptor tyrosine kinase expressed by human lymphoid tumor cell lines.Proceedings of the National Academy of Sciences of the United States of America · 1992
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

E B PasqualeDepartment of Biology, University of California, San Diego, La Jolla 92093.
University of California San Diego · US

Funding

DEVELOPMENTAL BIOLOGY OF EPH-RELATED TYROSINE KINASESR01HD026351 · NICHD · BURNHAM INSTITUTE FOR MEDICAL RESEARCH · PI PASQUALE, ELENA B · 1995 to 1999
–
DEVELOPMENTAL BIOLOGY OF PROTEIN TYROSINE KINASESR29HD026351 · NICHD · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI PASQUALE, ELENA B · 1990 to 1994
–
NICHD NIH HHS HD-26351NIGMS NIH HHS GM-15971
6 · The paper itself

Abstract

Chicken embryo kinase 5 (Cek5) is a transmembrane tyrosine kinase of the Eph family that was identified by screening a 10-d chicken embryo cDNA expression library with anti-phosphotyrosine antibodies. The extracellular region of Cek5 contains a cysteine rich N-terminal subdomain and a C-terminal subdomain mostly devoid of cysteines and comprising two repeats similar to fibronectin type III repeats. Immunoblotting experiments with anti-Cek5 polyclonal antibodies indicated that Cek5 is a membrane-associated 120-kDa protein containing intramolecular (but not intermolecular) disulfide bonds. Cek5 is already expressed in 2-d-old chicken embryos and is also expressed, at higher levels, later in development. In 10-d-old chicken embryos, Cek5 is expressed at substantial levels in nearly all the tissues examined, whereas in adult it is expressed predominantly in the brain. The expression of Cek5 in the brain gradually diminishes during embryonic development, whereas in the skeletal muscle of the thigh a sharp decrease in Cek5 expression was detected at the time of terminal muscle differentiation. Its wide tissue distribution throughout development and its sustained expression in adult brain suggest that Cek5 is an important component of signal transduction pathways, likely to interact with a widely distributed and important ligand, which is as yet unknown.

Indexed as

Amino Acid SequenceAnimalsBase SequenceChick EmbryoGene Expression Regulation, EnzymologicHistocompatibility Antigens Class IIMolecular Sequence DataOpen Reading FramesProtein-Tyrosine KinasesReceptor, EphB2Receptors, Cell SurfaceSequence AlignmentSignal TransductionHistocompatibility Antigens Class IIIa-like antigens, avianProtein-Tyrosine KinasesReceptor, EphB2Receptors, Cell Surface

Identifiers

PMID1664238
PMCPMC361842
OpenAlexW2023381747

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.